ID   DYHC_PARTE              Reviewed;        4540 AA.
AC   Q27171; Q6LED7;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Dynein heavy chain, cytoplasmic;
DE   AltName: Full=DHC08;
DE   AltName: Full=Dynein heavy chain, cytosolic;
DE            Short=DYHC;
GN   Name=DHC-8;
OS   Paramecium tetraurelia.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Stock 51;
RX   PubMed=8589455; DOI=10.1091/mbc.6.11.1549;
RA   Kandl K.A., Forney J.D., Asai D.J.;
RT   "The dynein genes of Paramecium tetraurelia: the structure and expression
RT   of the ciliary beta and cytoplasmic heavy chains.";
RL   Mol. Biol. Cell 6:1549-1562(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1836-1889.
RC   STRAIN=Stock 51;
RX   PubMed=8056840; DOI=10.1242/jcs.107.4.839;
RA   Asai D.J., Beckwith S.M., Kandl K.A., Keating H.H., Tjandra H.,
RA   Forney J.D.;
RT   "The dynein genes of Paramecium tetraurelia. Sequences adjacent to the
RT   catalytic P-loop identify cytoplasmic and axonemal heavy chain isoforms.";
RL   J. Cell Sci. 107:839-847(1994).
CC   -!- FUNCTION: Cytoplasmic dynein acts as a motor for the intracellular
CC       retrograde motility of vesicles and organelles along microtubules.
CC       Dynein has ATPase activity; the force-producing power stroke is thought
CC       to occur on release of ADP.
CC   -!- SUBUNIT: Consists of at least two heavy chains and a number of
CC       intermediate and light chains.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- DOMAIN: Dynein heavy chains probably consist of an N-terminal stem
CC       (which binds cargo and interacts with other dynein components), and the
CC       head or motor domain. The motor contains six tandemly-linked AAA
CC       domains in the head, which form a ring. A stalk-like structure (formed
CC       by two of the coiled coil domains) protrudes between AAA 4 and AAA 5
CC       and terminates in a microtubule-binding site. A seventh domain may also
CC       contribute to this ring; it is not clear whether the N-terminus or the
CC       C-terminus forms this extra domain. There are four well-conserved and
CC       two non-conserved ATPase sites, one per AAA domain. Probably only one
CC       of these (within AAA 1) actually hydrolyzes ATP, the others may serve a
CC       regulatory function.
CC   -!- SIMILARITY: Belongs to the dynein heavy chain family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U20449; AAA75445.1; -; Genomic_DNA.
DR   EMBL; L17132; AAA61606.1; -; mRNA.
DR   PIR; T30838; T30838.
DR   SMR; Q27171; -.
DR   STRING; 5888.CAK78975; -.
DR   eggNOG; KOG3595; Eukaryota.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008569; F:minus-end-directed microtubule motor activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   Gene3D; 1.10.8.710; -; 1.
DR   Gene3D; 1.10.8.720; -; 1.
DR   Gene3D; 1.20.140.100; -; 1.
DR   Gene3D; 3.10.490.20; -; 1.
DR   Gene3D; 3.20.180.20; -; 1.
DR   Gene3D; 3.40.50.300; -; 5.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR035699; AAA_6.
DR   InterPro; IPR035706; AAA_9.
DR   InterPro; IPR041658; AAA_lid_11.
DR   InterPro; IPR042219; AAA_lid_11_sf.
DR   InterPro; IPR041589; DNAH3_AAA_lid_1.
DR   InterPro; IPR042222; Dynein_2_N.
DR   InterPro; IPR043157; Dynein_AAA1S.
DR   InterPro; IPR041466; Dynein_AAA5_ext.
DR   InterPro; IPR041228; Dynein_C.
DR   InterPro; IPR043160; Dynein_C_barrel.
DR   InterPro; IPR024743; Dynein_HC_stalk.
DR   InterPro; IPR024317; Dynein_heavy_chain_D4_dom.
DR   InterPro; IPR004273; Dynein_heavy_D6_P-loop.
DR   InterPro; IPR013602; Dynein_heavy_linker.
DR   InterPro; IPR013594; Dynein_heavy_tail.
DR   InterPro; IPR042228; Dynein_linker_3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF12774; AAA_6; 1.
DR   Pfam; PF12780; AAA_8; 1.
DR   Pfam; PF12781; AAA_9; 1.
DR   Pfam; PF17857; AAA_lid_1; 1.
DR   Pfam; PF18198; AAA_lid_11; 1.
DR   Pfam; PF08385; DHC_N1; 1.
DR   Pfam; PF08393; DHC_N2; 1.
DR   Pfam; PF17852; Dynein_AAA_lid; 1.
DR   Pfam; PF18199; Dynein_C; 1.
DR   Pfam; PF03028; Dynein_heavy; 1.
DR   Pfam; PF12777; MT; 1.
DR   SMART; SM00382; AAA; 3.
DR   SUPFAM; SSF52540; SSF52540; 4.
PE   2: Evidence at transcript level;
KW   ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Dynein; Microtubule;
KW   Motor protein; Nucleotide-binding; Repeat.
FT   CHAIN           1..4540
FT                   /note="Dynein heavy chain, cytoplasmic"
FT                   /id="PRO_0000114641"
FT   REGION          1..1796
FT                   /note="Stem"
FT                   /evidence="ECO:0000250"
FT   REGION          1797..2018
FT                   /note="AAA 1"
FT                   /evidence="ECO:0000250"
FT   REGION          2091..2348
FT                   /note="AAA 2"
FT                   /evidence="ECO:0000250"
FT   REGION          2457..2705
FT                   /note="AAA 3"
FT                   /evidence="ECO:0000250"
FT   REGION          2796..3056
FT                   /note="AAA 4"
FT                   /evidence="ECO:0000250"
FT   REGION          3076..3367
FT                   /note="Stalk"
FT                   /evidence="ECO:0000250"
FT   REGION          3140..3159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3444..3673
FT                   /note="AAA 5"
FT                   /evidence="ECO:0000250"
FT   REGION          3908..4123
FT                   /note="AAA 6"
FT                   /evidence="ECO:0000250"
FT   COILED          440..482
FT                   /evidence="ECO:0000255"
FT   COILED          698..722
FT                   /evidence="ECO:0000255"
FT   COILED          794..827
FT                   /evidence="ECO:0000255"
FT   COILED          975..995
FT                   /evidence="ECO:0000255"
FT   COILED          1169..1251
FT                   /evidence="ECO:0000255"
FT   COILED          1295..1311
FT                   /evidence="ECO:0000255"
FT   COILED          3076..3182
FT                   /evidence="ECO:0000255"
FT   COILED          3289..3367
FT                   /evidence="ECO:0000255"
FT   COILED          3653..3688
FT                   /evidence="ECO:0000255"
FT   COILED          3820..3851
FT                   /evidence="ECO:0000255"
FT   COILED          4238..4259
FT                   /evidence="ECO:0000255"
FT   COILED          4313..4342
FT                   /evidence="ECO:0000255"
FT   BINDING         1835..1842
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2129..2136
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2496..2503
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2834..2841
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   4540 AA;  528637 MW;  0C6103148BFB95F9 CRC64;
     MEESETQLNV KVQEQGKLYS ANEIENFNQY LSAICLSLLI IDKDQWNVAC HEDVNQQNIC
     QFLSDSQIKA LIVSKTVENE KFNIQIRSEY EASNNYAHTI CFLKRHTFQY DNQLQPQQFS
     NHVQVINVGY AESQGGANPF TLSHNYVQNC FIPIFTQYKG EIDKKRIVDQ SSYNDLIKKL
     NEVNLAFIKC RQNVEVPEII LQFDPRIKEA VKQRGGKPTI EDAAQLNKPD IVQSISQTVT
     RWISDINQIS NTKLELTNAS IVDEINYWMS MERSLFFIEN QLKQPEVDFT IEVLTQAKKM
     NITAQFKEIA LKQSLQKCQS CNQFMKEFPI NNLLIATNLV EIKDAMIQIF QHMKKLSNIQ
     ETYTIPRSLQ LAESFSRELT NEMIKYFKGF QILHIKYVDF KGLIIKTQEI FSQWDEEYKI
     FKQSIVKKSV HQKDQYGQFE HIKLQKQIQH IQRLREMHEN LKEVIEQIIQ NDQEEQKENV
     QQFATLQEIQ QAYDIFKNVE VFDLSRDGED QFFRALKQYE IAIESVEATI TTNLRDSLGS
     ASSAKEMFRI LAKFNKLFSR PRIKGAIQEY QSQLLKTVHK DIQSLQNKFK ETYQKSQNSR
     LASARDIPLT SGFVIWSKQL QIRLQKYMQK VEQILGPQWA EDTDGKKCKE MGETFERILD
     SGPALEDWKQ EINHHNKAVS QNEKLFEVVT RRRGLEIRVN YEKKLSQLFK EVRNLSNMKT
     KVPYSISHIA NDAKASYPFA LSLQESLHTY IQITSQLNAK SAKLVAALRK EVQLQIGQGF
     NYLWTHKTQL QPYVKKFTDK VFELEQAVNG LNERIGQIES LCEAMKTCPV DSLADKLKDI
     QEVIDSLCFN NFSNLHIWIQ DIDKQIESIL CDRVTVQMKE WLNQFINYQK IQERGLVNQT
     VVHELKLQDQ IIYVDPPVEY AKYFWFQEFH KMIGQICSLP RLVANRFDNT IQQNTGPWGT
     QRDLDYSTTI NKINQQLIKD AYSQIGQLLE DMEQYVQTWL NYQSLWELDI KQVEQILQDD
     IEKWQQMLTD IKQGRATFDN STTEEHFGAI IIDYRMVQVK INHKYDAWHK ELLNHFGNKF
     GEQLRVFNKN VTTEKEKLLK INFQDLTSDI IESITIIQEQ DKKFPGWSAD IESFKNGQKV
     LDRQRYQYPG DWLSFEQVEM QWNQFKQIRS KKLQSQESEM NNIQSKIQQD ERYLNQQIQE
     IEEQWKTSKP DSGDCSPNEA EQILKSLNEQ LISVQEKYEK CSQAKEILKM DPPTHQQKLN
     VLLESISDLQ DVWQELGKIW KVMQSIKEQL ISALQNKKIK DTCDEAQKQL NGVSTKTRNY
     DAFEKMKEKV KNYIKMNKLI MDLKDESMKE RHWRQLLSKL KINESLNQLQ MQHLWNANLL
     NYENLAKDIM TVARGEQVLE TMISQVKDFW NSFELELVKY QTKCKLIRGW DELFQKLDED
     LNNLASMKIS PFYKTFEAEI SQWDDKLQKV KLTMDIWIDV QRRWVYLEGI FFGSSDIKTQ
     LQNEYNKFKD IDSQFTNLMK KVAQKPQLMD VQGIPNLAKT LERLSDFLQK IQKALGDYLE
     TQRQAFARFY FVGDDDLLDI IGNSKDVTNV QRHFPKMYAG IVQLQSRKDG NDDVVLGMSS
     KEGEVVPFSK EVKIAEDPRI NIWLGKVDNE MMNSLALDLE KSVLDIQANQ QNRMKVIEEH
     PAQIILLALQ VGWCFSVESS FNNEQQMKQT LQYVLEFLSE LAESVLKDHP KQLRQKFEQI
     ITDFVHQRDV IRLLMNNKIN SKNDFGWQYH MRFNWNSKEA DPGKRLLIQM GNAQFHYGFE
     YLGVAEKLVQ TPLTDKCFLT LTQALHLRMG GSPFGPAGTG KTESVKALGA QLGRFVLVFN
     CDETFDFNAM GRIFVGLCQV GAWGCFDEFN RLEERMLSAC SQQILLIQTG LREKQKQIEL
     MGKDVKLSSQ MGVFVTMNPG YAGRSNLPEN LKQLFRQMAM VKPDRELIAQ VMLFSQGFRT
     AEKLAGKIVS LFELCDNQLS SQPHYDFGLR ALKSVLNSAG NMKRQEMIDR KQEPVPQSEI
     EEFEQTILLR SVCDTVVPKL IKDDIKLLET LLQGVFPGSC IPEIKEEQLR KELALACQRK
     NLQSSKNFIE KVLQLYQIQR LQHGLMLVGP CGCGKSAAWR VLLEAMYKCD KVKGEFYIVD
     PKAISKDELY GRLDNTTLEW TDGVFTSILR KIISNQRQES TRRHWIIFDG DVDPEWAENL
     NSVLDDNKLL TLPNGERLAI PPNVRMIFEV ETLKYATLAT VSRCGMVWFS EETINDENIF
     YHFLERLKQD DYDQQKSEDD NNKQVNSQES ELRTKCVKAL ESIIKFLSQF LQIAQKPEYK
     HVMEFTRIRV LESTFALVRR SISNIIEYNE NNSEVPLEDD QINDFMVKQF LIAVMWGVAG
     SMNLYQRTQY SKEICQLLPH NVILPQFNDS APSLIDFEVT LPEAQWSQYK KKVPQIEIDP
     QRVTDADLII ETVDTLRHKD VLCGWLNEHR PFLLCGPPGS GKTMTLMSTL KALTDFEMIF
     INFSSSTMPQ LIIKQFDHYC EYKKTTNGVF LQPKNQKWLV VFCDEINLPD QDKYGTMAII
     TFLRQLTEQH GFWRSSDRQW ISLDRIQFVG ACNPPTDVGR KPLTPRFLRH CPLILVDFPG
     PESLKQIYGT FNKAMLRRTV NLKQYSEQLT NAMVEFYTKS QQHFTADQQA HYIYSPRELT
     RWKYALNEAL EPLESVEDLV RLWAHEGLRL FQDRLVHEHE KEWCNKLIDQ VAYNNFNNLK
     DEALQRPILF SNYLHKVYQS VDREELRKYI QGRLKQFNEE ELSVPLVVFD DVLDHILRID
     RVLKQPLGHL LLVGSSGVGK TTLTRFVSWI NNLTVFQIKA GRDYQLADFD NDLREVMKRA
     GAKGEKITFI FDESNVLGPS FLEKMNALLA SGEIPGLFEN DEYLALINLL KENSNQNKQF
     DSSEEQLFKN FTYQVQRNLH VVFTMNPKNP DFSNRTASSP ALFNRCVIDW FGDWTNEALF
     QVGKAFTMYI DPPENAFSKK IKDETQRQHI LVSTLVYIQN TIIELNNKLQ KGAKRFNYIT
     PRDYLDFLKH FEKLHNEKKS QLEDQQLHLN VGLDKLKETE QQVLEMQKSL DQKKVELLTK
     ERQAGEKLQT IIEEKKIAEK KKEDSTRLSS DAEKKAKEME VRQSQVNKEL NEALPALENA
     KQCVNSIKKD DLNQIRALGS PPALVKLTME AVVCAINSLE KSPEWKDVQK SMANMNFINN
     VINFNTETMP PKVKKFILTK YLSAQEWNID RINFASKAAG PLAMWLDSQL KYADILQKVD
     PLRQEVAKLL QESDELNTQK KIYDDEVAAA EAKIHNLQQE YSELISQKES IKSEMLKVQE
     KVTRSQALLS DLSGERVRWE EASQNFKSQL ATMIGDVLLL LAIPVLYWVL DHFYRKVVIN
     TWKDYLSGQA NIFYRQDLSL IEFLSRPSDR LNWQLHTLPS DDLCMENAII LYRFQRYPLV
     IDPSGQALSF ISSLYKDKKL ARTSFTDESF LKTLETCLRF GCPLLVQDVE KVDPILNSVL
     NNETYKTGGR VLIRVGNQEI DFSQGFTMFM ITRDSTARFT PDLCSRVTFV NFTVTQSSLQ
     EQCLNIFLRN ESPETEEKRL NLMKLQGEYI VKLRELEDQL LDSLNNSRGS ILEDEKVIQT
     LEKLKKEAAV IVQEMKQADT IMNEVMNTTH SYVPLANTTS KIFFSLTSLA NIHYLYQFSL
     QFFMDTIYNV LNKNEQLQKI PKQDLIKRRI LIFNEMFKEI YKRMNFSLLQ EDKLVFAITL
     AQVKLGDNTL GQEFLNVFKP PTVMETTFSN TFLQGKLSIQ QLKQLEGITQ QNQTFNRLID
     NLNKNEDRWL NFLNDEAPEN DIPTQWYNEV QRDDIVKLDW IDSHQLKRQL DDLHILRIFR
     ADRFQIIARK LINQILGEGF MDEQTVDMKL VVEKEASNKI PILLCSAPGF DPSFKVEQLS
     REMGIKLTSV AIGSAEGFDQ AEYEITQSVK SGSWVMLKNV HLATSWLNDL EKKLFRLTPN
     ANFRIFLTME FNPKIPTTLI RQSYKLVFEP PDGIKASLIR TFKTVLSQQR TDRQPVERAR
     LHFLLAWLHA VILERLRFTP IGWSKTYEFN EADQRCSLDL IDEYVDALGI RQNIDPSKLP
     WDAFRTILTQ NLYGGKVDNE YDQKILQSLV EQFFTEQSFN HNHPLFFTLE GKEAITVPEG
     RTYLDFMQWI EQLPKTESPE WSGLPSNVER VQRDQLTQKL ITKVQNLQQE GEEEITQIEV
     QTEKTQKKDN KKSDQVQWLQ DLLEKVEKFK AILPNKISPL ERTADSINDP LFRFLDREIT
     VASKLLKAVR QNIEELIQLA QGKILATNIL RQLAKDVFNN IVPAQWNKYN VITMPLNDWV
     GDFKRRIDQF DLLGKTKDFQ KGQVWFGGLL FPEAYLTATR QYVAQANKWS LEELELQMIP
     EDQGIDEDSF VIEGVSMEGG HLDSKTLQVR IVNEISVALK PITLKWCKTS QKGVVGDDEI
     VLPVYLNKTR KNLIFSLKVK MGKLNRYTLY QKGLSFILFN